Factor Xa: Difference between revisions
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===Heavy Chain=== | ===Heavy Chain=== | ||
[[Image:Greek_key_barrel_arrows.png|thumb|200px|Greek Key barrel.]] | [[Image:Greek_key_barrel_arrows.png|thumb|200px|Greek Key barrel.]] | ||
The factor Xa heavy chain contains the activation peptide (no crystal structures of inactive Factor X containing the activation peptide have been solved) and the trypsin-like serine protease domain | The factor Xa heavy chain contains the activation peptide (no crystal structures of inactive Factor X containing the activation peptide have been solved) and the trypsin-like serine protease domain. | ||
The members of the trypsin-like serine protease family have two homologous greek key β-barrel subdomains (<scene name='Factor_Xa/Transparent_-no_inhib-_barrel1/1'>barrel 1</scene>, <scene name='Factor_Xa/Transparent_-_no_inhib_barrel2/1'>barrel 2</scene>) in the heavy chain. The greek key barrel is characterized as an up and down β-barrel with an n+3 linkage across the barrel, in this case, the across barrel linkage is an α-helix. The <scene name='Factor_Xa/Transparent_-no_inhib-_barrels/1'>two barrels</scene> pack together asymmetrically to constitute the compact <scene name='Factor_Xa/Transparent_-_barrels_catalyt/1'>catalytic domain</scene> (see below for more information). Although the hydrophobic core structures remain conserved throughout the family (12), considerable variation is seen in the surface loops, especially surrounding the active site where they determine substrate specificities. <ref>PMID: 9707558</ref> | The members of the trypsin-like serine protease family have two homologous greek key β-barrel subdomains (<scene name='Factor_Xa/Transparent_-no_inhib-_barrel1/1'>barrel 1</scene>, <scene name='Factor_Xa/Transparent_-_no_inhib_barrel2/1'>barrel 2</scene>) in the heavy chain. The greek key barrel is characterized as an up and down β-barrel with an n+3 linkage across the barrel, in this case, the across barrel linkage is an α-helix. The <scene name='Factor_Xa/Transparent_-no_inhib-_barrels/1'>two barrels</scene> pack together asymmetrically to constitute the compact <scene name='Factor_Xa/Transparent_-_barrels_catalyt/1'>catalytic domain</scene> (see below for more information). Although the hydrophobic core structures remain conserved throughout the family (12), considerable variation is seen in the surface loops, especially surrounding the active site where they determine substrate specificities. <ref>PMID: 9707558</ref> | ||